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Literature summary for 4.1.1.23 extracted from

  • Bello, A.M.; Poduch, E.; Fujihashi, M.; Amani, M.; Li, Y.; Crandall, I.; Hui, R.; Lee, P.I.; Kain, K.C.; Pai, E.F.; Kotra, L.P.
    A potent, covalent inhibitor of orotidine 5-monophosphate decarboxylase with antimalarial activity (2007), J. Med. Chem., 50, 915-921.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
6-iodouridine 5'-monophosphate i.e. 6-iodo-UMP, irreversible inhibition, mass spectral analysis of the enzyme-inhibitor complex, binding to the enzyme is accompanied by loss of two protons and the iodo moiety, covalent bond formation Methanothermobacter thermautotrophicus
6-iodouridine 5'-monophosphate i.e. 6-iodo-UMP, irreversible inhibition, mass spectral analysis of the enzyme-inhibitor complex, binding to the enzyme is accompanied by loss of two protons and the iodo moiety, covalent bond formation, the inhibitor exhibits potent antiplasmodial activity Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Orotidine 5'-phosphate Methanothermobacter thermautotrophicus
-
UMP + CO2
-
?
Orotidine 5'-phosphate Plasmodium falciparum
-
UMP + CO2
-
?

Organism

Organism UniProt Comment Textmining
Methanothermobacter thermautotrophicus
-
-
-
Plasmodium falciparum Q8IJH3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Orotidine 5'-phosphate
-
Methanothermobacter thermautotrophicus UMP + CO2
-
?
Orotidine 5'-phosphate
-
Plasmodium falciparum UMP + CO2
-
?
Orotidine 5'-phosphate the enzyme catalyzes the decarboxylation of orotidine 5'-monophosphate without any covalent intermediates, active site residues in ODCase are involved in an extensive hydrogen-bonding network, active site Lys42 Methanothermobacter thermautotrophicus UMP + CO2
-
?
Orotidine 5'-phosphate the enzyme catalyzes the decarboxylation of orotidine 5'-monophosphate without any covalent intermediates, active site residues in ODCase are involved in an extensive hydrogen-bonding network, active site Lys42 Plasmodium falciparum UMP + CO2
-
?

Synonyms

Synonyms Comment Organism
ODCase
-
Methanothermobacter thermautotrophicus
ODCase
-
Plasmodium falciparum
orotidine 5-monophosphate decarboxylase
-
Methanothermobacter thermautotrophicus
orotidine 5-monophosphate decarboxylase
-
Plasmodium falciparum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Methanothermobacter thermautotrophicus
22
-
assay at room temperature Plasmodium falciparum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Methanothermobacter thermautotrophicus
7.5
-
assay at Plasmodium falciparum

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0044 0.0062 pH 7.5, 22°C, with different Plasmodium falciparum isolates Plasmodium falciparum 6-iodo-UMP